CO4A2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CO4A2_HUMAN
• UniProt AC: P08572
• Protein Name: Collagen alpha-2(IV) chain
• Gene Name: COL4A2
• Organism: Homo sapiens (Human).
• Sequence Length: 1712
• Subcellular Localization: Secreted, extracellular space, extracellular matrix, basement membrane.
• Protein Description: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.; Canstatin, a cleavage product corresponding to the collagen alpha 2(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor cell activity. It inhibits proliferation and migration of endothelial cells, reduces mitochondrial membrane potential, and induces apoptosis. Specifically induces Fas-dependent apoptosis and activates procaspase-8 and -9 activity. Ligand for alphavbeta3 and alphavbeta5 integrins..
• Protein Sequence: MGRDQRAVAGPALRRWLLLGTVTVGFLAQSVLAGVKKFDVPCGGRDCSGGCQCYPEKGGRGQPGPVGPQGYNGPPGLQGFPGLQGRKGDKGERGAPGVTGPKGDVGARGVSGFPGADGIPGHPGQGGPRGRPGYDGCNGTQGDSGPQGPPGSEGFTGPPGPQGPKGQKGEPYALPKEERDRYRGEPGEPGLVGFQGPPGRPGHVGQMGPVGAPGRPGPPGPPGPKGQQGNRGLGFYGVKGEKGDVGQPGPNGIPSDTLHPIIAPTGVTFHPDQYKGEKGSEGEPGIRGISLKGEEGIMGFPGLRGYPGLSGEKGSPGQKGSRGLDGYQGPDGPRGPKGEAGDPGPPGLPAYSPHPSLAKGARGDPGFPGAQGEPGSQGEPGDPGLPGPPGLSIGDGDQRRGLPGEMGPKGFIGDPGIPALYGGPPGPDGKRGPPGPPGLPGPPGPDGFLFGLKGAKGRAGFPGLPGSPGARGPKGWKGDAGECRCTEGDEAIKGLPGLPGPKGFAGINGEPGRKGDRGDPGQHGLPGFPGLKGVPGNIGAPGPKGAKGDSRTITTKGERGQPGVPGVPGMKGDDGSPGRDGLDGFPGLPGPPGDGIKGPPGDPGYPGIPGTKGTPGEMGPPGLGLPGLKGQRGFPGDAGLPGPPGFLGPPGPAGTPGQIDCDTDVKRAVGGDRQEAIQPGCIGGPKGLPGLPGPPGPTGAKGLRGIPGFAGADGGPGPRGLPGDAGREGFPGPPGFIGPRGSKGAVGLPGPDGSPGPIGLPGPDGPPGERGLPGEVLGAQPGPRGDAGVPGQPGLKGLPGDRGPPGFRGSQGMPGMPGLKGQPGLPGPSGQPGLYGPPGLHGFPGAPGQEGPLGLPGIPGREGLPGDRGDPGDTGAPGPVGMKGLSGDRGDAGFTGEQGHPGSPGFKGIDGMPGTPGLKGDRGSPGMDGFQGMPGLKGRPGFPGSKGEAGFFGIPGLKGLAGEPGFKGSRGDPGPPGPPPVILPGMKDIKGEKGDEGPMGLKGYLGAKGIQGMPGIPGLSGIPGLPGRPGHIKGVKGDIGVPGIPGLPGFPGVAGPPGITGFPGFIGSRGDKGAPGRAGLYGEIGATGDFGDIGDTINLPGRPGLKGERGTTGIPGLKGFFGEKGTEGDIGFPGITGVTGVQGPPGLKGQTGFPGLTGPPGSQGELGRIGLPGGKGDDGWPGAPGLPGFPGLRGIRGLHGLPGTKGFPGSPGSDIHGDPGFPGPPGERGDPGEANTLPGPVGVPGQKGDQGAPGERGPPGSPGLQGFPGITPPSNISGAPGDKGAPGIFGLKGYRGPPGPPGSAALPGSKGDTGNPGAPGTPGTKGWAGDSGPQGRPGVFGLPGEKGPRGEQGFMGNTGPTGAVGDRGPKGPKGDPGFPGAPGTVGAPGIAGIPQKIAVQPGTVGPQGRRGPPGAPGEMGPQGPPGEPGFRGAPGKAGPQGRGGVSAVPGFRGDEGPIGHQGPIGQEGAPGRPGSPGLPGMPGRSVSIGYLLVKHSQTDQEPMCPVGMNKLWSGYSLLYFEGQEKAHNQDLGLAGSCLARFSTMPFLYCNPGDVCYYASRNDKSYWLSTTAPLPMMPVAEDEIKPYISRCSVCEAPAIAIAVHSQDVSIPHCPAGWRSLWIGYSFLMHTAAGDEGGGQSLVSPGSCLEDFRATPFIECNGGRGTCHYYANKYSFWLTTIPEQSFQGSPSADTLKAGLIRTHISRCQVCMKNL

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
42	S-palmitoylation	VKKFDVPCGGRDCSG CCCCCCCCCCCCCCC	10.17	21044946
111	O-linked_Glycosylation	DVGARGVSGFPGADG CCCCCCCCCCCCCCC	37.22	55826745
138	N-linked_Glycosylation	RPGYDGCNGTQGDSG CCCCCCCCCCCCCCC	63.17	3198637
265	O-linked_Glycosylation	LHPIIAPTGVTFHPD CCCEECCCCCEECHH	34.95	OGP
306	Phosphorylation	GFPGLRGYPGLSGEK CCCCCCCCCCCCCCC	6.41	22817900
321	Phosphorylation	GSPGQKGSRGLDGYQ CCCCCCCCCCCCCCC	30.15	-
327	Phosphorylation	GSRGLDGYQGPDGPR CCCCCCCCCCCCCCC	15.23	-
327	Nitration	GSRGLDGYQGPDGPR CCCCCCCCCCCCCCC	15.23	-
453	Acetylation	DGFLFGLKGAKGRAG CCEEECCCCCCCCCC	58.14	30587807
456	Acetylation	LFGLKGAKGRAGFPG EECCCCCCCCCCCCC	58.56	30587813
467	Phosphorylation	GFPGLPGSPGARGPK CCCCCCCCCCCCCCC	20.44	29214152
1002	Acetylation	DEGPMGLKGYLGAKG CCCCCCHHHHHCCCC	39.52	12655523
1081	Nitration	APGRAGLYGEIGATG CCCCCCCCCCCCCCC	16.28	-
1081	Phosphorylation	APGRAGLYGEIGATG CCCCCCCCCCCCCCC	16.28	22210691
1096	Phosphorylation	DFGDIGDTINLPGRP CCCCCCCCCCCCCCC	13.42	22210691
1204	Phosphorylation	GLHGLPGTKGFPGSP CCCCCCCCCCCCCCC	26.50	22468782
1303	Phosphorylation	GPPGPPGSAALPGSK CCCCCCCCCCCCCCC	19.01	-
1309	Phosphorylation	GSAALPGSKGDTGNP CCCCCCCCCCCCCCC	31.37	-
1313	Phosphorylation	LPGSKGDTGNPGAPG CCCCCCCCCCCCCCC	47.75	-
1361	O-linked_Glycosylation	FMGNTGPTGAVGDRG CCCCCCCCCCCCCCC	38.83	55832591
1403	O-linked_Glycosylation	KIAVQPGTVGPQGRR EEEECCCCCCCCCCC	29.04	20068231
1403	Phosphorylation	KIAVQPGTVGPQGRR EEEECCCCCCCCCCC	29.04	20068231
1446	O-linked_Glycosylation	PQGRGGVSAVPGFRG CCCCCCCCCCCCCCC	27.16	37819195
1446	Phosphorylation	PQGRGGVSAVPGFRG CCCCCCCCCCCCCCC	27.16	21406692
1475	Phosphorylation	GAPGRPGSPGLPGMP CCCCCCCCCCCCCCC	20.62	28857561
1485	Phosphorylation	LPGMPGRSVSIGYLL CCCCCCCEEEEEEEE	26.57	21712546
1564	Phosphorylation	YASRNDKSYWLSTTA EECCCCCCEEEECCC	25.14	20068231
1565	Phosphorylation	ASRNDKSYWLSTTAP ECCCCCCEEEECCCC	18.99	20068231
1568	Phosphorylation	NDKSYWLSTTAPLPM CCCCEEEECCCCCCC	15.01	20068231
1569	Phosphorylation	DKSYWLSTTAPLPMM CCCEEEECCCCCCCC	25.47	20068231
1570	Phosphorylation	KSYWLSTTAPLPMMP CCEEEECCCCCCCCC	23.93	20068231
1586	Phosphorylation	AEDEIKPYISRCSVC CHHHCHHHHCCCCCC	13.41	20068231
1588	Phosphorylation	DEIKPYISRCSVCEA HHCHHHHCCCCCCCC	22.76	20068231
1624	Phosphorylation	RSLWIGYSFLMHTAA HEEEEEEEEEECCCC	13.49	22210691
1683	Phosphorylation	LTTIPEQSFQGSPSA EEECCHHHCCCCCCH	20.20	-
1687	Phosphorylation	PEQSFQGSPSADTLK CHHHCCCCCCHHHHH	12.61	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CO4A2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CO4A2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CO4A2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CO4A2_HUMAN	COL4A2	physical	12011424
CO4A1_HUMAN	COL4A1	physical	12011424
TNPO3_HUMAN	TNPO3	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 614483: Porencephaly 2 (POREN2)
• 614519: Intracerebral hemorrhage (ICH)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"The complete primary structure of the alpha 2 chain of human type IVcollagen and comparison with the alpha 1(IV) chain.";
Hostikka S.L., Tryggvason K.;
J. Biol. Chem. 263:19488-19493(1988).
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
PubMed: 3198637